Autor: |
Inoue, J, Kerr, L D, Ransone, L J, Bengal, E, Hunter, T, Verma, I M |
Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; May 1991, Vol. 88 Issue: 9 p3715-3719, 5p |
Abstrakt: |
We show that the product of the protooncogene c-rel is a constituent of an NF-kappa B-like complex that binds to the kappa B site originally identified in the enhancer of immunoglobulin kappa light chain gene. c-rel protein synthesized in bacteria binds to the kappa B site in a sequence-specific manner. The rel-kappa B complex can be disrupted by incubation with anti-rel antibodies. The rel protein can form oligomers. The c-rel protein can activate transcription from promoters containing kappa B sites; v-rel, on the other hand, suppresses the transcription of genes linked to kappa B sites. Thus, v-rel may interfere with the normal transcriptional machinery of the cell by acting as a dominant negative mutant. |
Databáze: |
Supplemental Index |
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